Specificity of arginine binding by the Tetrahymena intron (original) (raw)

L-Arginine competitively inhibits the reaction of GTP with the Tetrahymena ribosomal self-splicing intron. In order to define this R N A binding site for arginine, Ki's have now been measured for numerous arginine-like competitive inhibitors. Detailed consideration of the Ki's suggests a tripartite binding model. L-and D-arginine from Chemical Dynamics, Fluka, and Sigma were compared without detectable differences. Guanidinoformic acid, guanidinoacetic acid, methylguanidine hydrochloride, ethylguanidine hydrochloride, butylguanidine hydrochloride, N"-acetyl-L-arginine, N"-benzoyl-L-arginyl ethyl ester, 6-guanidinocaproic acid, and 5-guanidinovaleric acid were obtained from Aldrich or the Bader Library of Rare Chemicals. L-2-Amino-3-guanidinopropionic acid and L-2amino-4-guanidinobutyric acid were from Chemical Dynamics. Guanylurea sulfate was obtained from Eastman Kodak. Agmatine, L-argininamide, L-arginine methyl ester, L-arginine ethyl ester, L-

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